Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Binding molecule specific for lrig-1 protein and use thereof

a technology of lrig-1 protein and binding molecule, which is applied in the field of binding molecule specific for lrig1 protein, can solve the problems of no genes and proteins that can target only the regulatory t cells alone, and achieve the effects of regulating immunological tolerance, and reducing the number of treg cells

Active Publication Date: 2020-04-30
GOOD T CELLS INC
View PDF0 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

The present invention provides a binding molecule, specifically an antibody, that targets the Lrig-1 protein. This molecule can activate the function of regulatory T cells, increase their number, and regulate immunological tolerance. This can effectively prevent, treat, or ameliorate immune-related diseases, such as autoimmune diseases, graft-versus-host diseases, organ transplant rejection, asthma, atopy, or inflammatory diseases, which are caused by excessive activation and expression of various immune cells and inflammatory cells. The binding molecule has been found to more effectively target the Lrig-1 protein and has good binding capacity.

Problems solved by technology

However, there are no genes and proteins that can target only the regulatory T cells alone.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Binding molecule specific for lrig-1 protein and use thereof
  • Binding molecule specific for lrig-1 protein and use thereof
  • Binding molecule specific for lrig-1 protein and use thereof

Examples

Experimental program
Comparison scheme
Effect test

preparation example 1

[Preparation Example 1] T Cell Subset Cell Culture

[0154]In order to identify whether the Lrig-1 protein is expressed only in regulatory T cells (Treg), the subsets of T cells, Th0, Th1, Th2, Th17, and iTreg, were prepared. The iTreg refers to cells whose differentiation has been artificially induced in a medium containing the following composition, unlike nTreg which has been naturally isolated.

[0155]The subsets of the T cells were induced to differentiate into respective cells by first isolating naive T cells obtained from the spleen of mice, causing RPMI1640 (Invitrogen Gibco, Grand Island, N.Y.) nutrient medium that contains 10% fetal bovine serum (FBS; HyClone, Logan, Utah) to further contain the respective ingredients of Table 1 below, and performing 72-hour incubation in an incubator at 37° C., 5% CO2.

TABLE 1Differentiated cellCompositionTh0anti-CD3, anti-CD28Th1IL-12, anti-IL-4 antibodyTh2IL-4, anti-IFNββTh17IL-6, TGFββ, anti-IFNββ, anti-IL-4iTregIL-2, TGFββ

example 1

[Example 1] Structural Analysis of Lrig-1

[0156]A three-dimensional steric structure of the extracellular domain of the Lrig-1 protein was predicted to produce antibodies specific for the Lrig-1 protein, a surface protein of regulatory T cells.

[0157]First, in order to predict base sequences of epitopes (epitopes), tools of Uniprot (http: / / www.uniprot.org) and RCSB Protein Data Bank (http: / / www.rcsb.org / pdb) were used to predict a three-dimensional steric structure of the extracellular domain (ECD) of the Lrig-1 protein so that the structure of ECD is identified. Then, the results are illustrated in FIGS. 1 and 2.

[0158]As illustrated in FIG. 1, a total of 15 leucine-rich regions of LRR1 to LRR15 existed in the Lrig-LRR domain (amino acid sequence at positions 41 to 494) in the extracellular domain of the Lrig-1 protein. Each of the LRR domains is composed of 23 to 27 amino acids, with 3 to 5 leucine being present.

[0159]In addition, as illustrated in FIG. 2, three immunoglobulin-like d...

example 2

[Example 2] Prediction of Lrig-1 Epitope Amino Acid Sequence

[0160]Prediction of the above base sequence was performed using Ellipro server (http: / / tools.iedb.org / ellipro / ) which is an epitope prediction software based on a structure of the Lrig-1 protein. The Ellipro search engine was used because it corresponds to a search engine known to be the most reliable among the existing algorithms for predicting an epitope.

[0161]The extracellular domain analyzed in Example 1 was entered into the epitope prediction software, and then predicted contiguous or discontiguous amino acid sequences of the predicted epitopes are illustrated in FIGS. 3 and 4.

[0162]As illustrated in FIGS. 3 and 4, a total of 22 contiguous epitope amino acid sequences were predicted, and a total of 8 discontiguous epitope amino acid sequences were predicted.

[Production Examples 1 to 4] Production of Monoclonal Antibodies Specific to Lrig-1 Protein

[0163]Antibodies specific for the Lrig-1 protein according to the present...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
structureaaaaaaaaaa
affinityaaaaaaaaaa
binding affinityaaaaaaaaaa
Login to View More

Abstract

The present invention relates to a binding molecule capable of specifically binding to Lrig-1 protein, which is located on the surface of a regulatory T cell. The binding molecule provided in the present invention can activate the function of regulatory T cells to effectively prevent, ameliorate, or treat diseases caused by excessive activation or expression of various immune cells and inflammatory cells, for example, immune-related diseases such as autoimmune disease, graft-versus-host disease, organ transplant rejection, asthma, atopy, acute or chronic inflammatory disease, etc. In addition, the binding molecule, preferably the antibody, specific for the Lrig-1 protein according to the present invention has advantages of more effectively targeting the Lrig-1 protein as compared with antibodies against Lrig-1 which are previously commercially available, and also possessing very good binding capacity thereto.

Description

TECHNICAL FIELD[0001]The present invention relates to a binding molecule capable of specifically binding to leucine-rich and immunoglobulin-like domains 1 (Lrig-1) protein, which is a protein present on the surface of regulatory T cells (Treg cells), and a use thereof.BACKGROUND ART[0002]One of the most important traits in all normal individuals is to have the ability to recognize and eliminate non-self antigens, while not detrimentally responding to antigenic substances that make up the self. As such, non-response of the living body to self antigens is called immunologic unresponsiveness or tolerance. Self-tolerance occurs by eliminating lymphocytes that may have specific receptors for self antigens, or by self-inactivation of the ability to respond after contacting self antigens. In a case where a problem arises in inducing or maintaining self-tolerance, an immune response to self antigens occurs, and the disease resulting therefrom is called autoimmune disease.[0003]For the treat...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Applications(United States)
IPC IPC(8): C07K16/28A61P37/06
CPCA61P37/06C07K16/28C07K2317/21C07K2317/565C07K2317/52C07K2317/622A61P35/00A61K2039/505C07K16/18C07K2317/76C07K2317/73
Inventor KIMKIM, BEOM SEOK
Owner GOOD T CELLS INC
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com